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Volumn 1792, Issue 7, 2009, Pages 664-675

A critical evaluation of the ubiquitin-proteasome system in Parkinson's disease

Author keywords

Aggregation; Alpha synuclein; DJ 1; Leucine rich repeat kinase 2; Lewy bodies; Parkin; Parkinson's disease; Substantia nigra; Ubiquitin ligase; Ubiquitin proteasome system

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; BRAIN DERIVED NEUROTROPHIC FACTOR; BRAIN DERIVED NEUROTROPHIC FACTOR RECEPTOR; CASEIN KINASE I; CASEIN KINASE II; CASPASE 3; CASPASE 8; DJ 1 PROTEIN; DOPAMINE RECEPTOR STIMULATING AGENT; FAS ANTIGEN; FAS ASSOCIATED DEATH DOMAIN PROTEIN; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN 90; HUNTINGTIN; INTERLEUKIN 1BETA CONVERTING ENZYME; KELCH LIKE ECH ASSOCIATED PROTEIN 1; LEUCINE RICH REPEAT KINASE 2; PARKIN; POLYGLUTAMINE; PRION PROTEIN; PROTEASOME; TAU PROTEIN; TRANSCRIPTION FACTOR NRF2; TYROSINE 3 MONOOXYGENASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UNINDEXED DRUG;

EID: 68649118090     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2009.01.012     Document Type: Review
Times cited : (94)

References (236)
  • 1
    • 0034973443 scopus 로고    scopus 로고
    • An algorithm (decision tree) for the management of Parkinson's disease (2001): treatment guidelines
    • Olanow C.W., Watts R.L., and Koller W.C. An algorithm (decision tree) for the management of Parkinson's disease (2001): treatment guidelines. Neurology 56 11 Suppl 5 (2001) S1-S88
    • (2001) Neurology , vol.56 , Issue.11 SUPPL. 5
    • Olanow, C.W.1    Watts, R.L.2    Koller, W.C.3
  • 2
    • 3142540683 scopus 로고    scopus 로고
    • Lewy-body formation is an aggresome-related process: a hypothesis
    • Olanow C.W., Perl D.P., DeMartino G.N., and McNaught K.S. Lewy-body formation is an aggresome-related process: a hypothesis. Lancet Neurol. 3 8 (2004) 496-503
    • (2004) Lancet Neurol. , vol.3 , Issue.8 , pp. 496-503
    • Olanow, C.W.1    Perl, D.P.2    DeMartino, G.N.3    McNaught, K.S.4
  • 3
    • 0032568534 scopus 로고    scopus 로고
    • alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
    • Spillantini M.G., Crowther R.A., Jakes R., Hasegawa M., and Goedert M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies. Proc. Natl. Acad. Sci. U. S. A. 95 11 (1998) 6469-6473
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.11 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 4
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos M.H., Lavedan C., Leroy E., Ide S.E., Dehejia A., Dutra A., et al. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276 5321 (1997) 2045-2047
    • (1997) Science , vol.276 , Issue.5321 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 5
    • 4644290985 scopus 로고    scopus 로고
    • Alpha-synuclein locus duplication as a cause of familial Parkinson's disease
    • Chartier-Harlin M.C., Kachergus J., Roumier C., Mouroux V., Douay X., Lincoln S., et al. Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364 9440 (2004) 1167-1169
    • (2004) Lancet , vol.364 , Issue.9440 , pp. 1167-1169
    • Chartier-Harlin, M.C.1    Kachergus, J.2    Roumier, C.3    Mouroux, V.4    Douay, X.5    Lincoln, S.6
  • 6
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
    • Kruger R., Kuhn W., Muller T., Woitalla D., Graeber M., Kosel S., et al. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease. Nat. Genet. 18 2 (1998) 106-108
    • (1998) Nat. Genet. , vol.18 , Issue.2 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 8
    • 10744230149 scopus 로고    scopus 로고
    • The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia
    • Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R., Ampuero I., et al. The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy body dementia. Ann. Neurol. 55 2 (2004) 164-173
    • (2004) Ann. Neurol. , vol.55 , Issue.2 , pp. 164-173
    • Zarranz, J.J.1    Alegre, J.2    Gomez-Esteban, J.C.3    Lezcano, E.4    Ros, R.5    Ampuero, I.6
  • 9
    • 41349084608 scopus 로고    scopus 로고
    • Patterns and stages of alpha-synucleinopathy: relevance in a population-based cohort
    • Zaccai J., Brayne C., McKeith I., Matthews F., and Ince P.G. Patterns and stages of alpha-synucleinopathy: relevance in a population-based cohort. Neurology 70 13 (2008) 1042-1048
    • (2008) Neurology , vol.70 , Issue.13 , pp. 1042-1048
    • Zaccai, J.1    Brayne, C.2    McKeith, I.3    Matthews, F.4    Ince, P.G.5
  • 10
    • 41149115508 scopus 로고    scopus 로고
    • Evidence that incidental Lewy body disease is pre-symptomatic Parkinson's disease
    • Dickson D.W., Fujishiro H., DelleDonne A., Menke J., Ahmed Z., Klos K.J., et al. Evidence that incidental Lewy body disease is pre-symptomatic Parkinson's disease. Acta Neuropathol. 115 4 (2008) 437-444
    • (2008) Acta Neuropathol. , vol.115 , Issue.4 , pp. 437-444
    • Dickson, D.W.1    Fujishiro, H.2    DelleDonne, A.3    Menke, J.4    Ahmed, Z.5    Klos, K.J.6
  • 12
    • 0025980627 scopus 로고
    • Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival
    • Heinemeyer W., Kleinschmidt J.A., Saidowsky J., Escher C., and Wolf D.H. Proteinase yscE, the yeast proteasome/multicatalytic-multifunctional proteinase: mutants unravel its function in stress induced proteolysis and uncover its necessity for cell survival. EMBO J. 10 3 (1991) 555-562
    • (1991) EMBO J. , vol.10 , Issue.3 , pp. 555-562
    • Heinemeyer, W.1    Kleinschmidt, J.A.2    Saidowsky, J.3    Escher, C.4    Wolf, D.H.5
  • 13
    • 0033016291 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and pathogenesis of human diseases
    • Schwartz A.L., and Ciechanover A. The ubiquitin-proteasome pathway and pathogenesis of human diseases. Annu. Rev. Med. 50 (1999) 57-74
    • (1999) Annu. Rev. Med. , vol.50 , pp. 57-74
    • Schwartz, A.L.1    Ciechanover, A.2
  • 14
    • 0038784529 scopus 로고    scopus 로고
    • Are ubiquitination pathways central to Parkinson's disease?
    • Giasson B.I., and Lee V.M. Are ubiquitination pathways central to Parkinson's disease?. Cell 114 1 (2003) 1-8
    • (2003) Cell , vol.114 , Issue.1 , pp. 1-8
    • Giasson, B.I.1    Lee, V.M.2
  • 17
    • 0032476030 scopus 로고    scopus 로고
    • Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants
    • Dick T.P., Nussbaum A.K., Deeg M., Heinemeyer W., Groll M., Schirle M., et al. Contribution of proteasomal beta-subunits to the cleavage of peptide substrates analyzed with yeast mutants. J. Biol. Chem. 273 40 (1998) 25637-25646
    • (1998) J. Biol. Chem. , vol.273 , Issue.40 , pp. 25637-25646
    • Dick, T.P.1    Nussbaum, A.K.2    Deeg, M.3    Heinemeyer, W.4    Groll, M.5    Schirle, M.6
  • 18
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev A.F., Akopian T.N., Castillo V., and Goldberg A.L. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4 3 (1999) 395-402
    • (1999) Mol. Cell , vol.4 , Issue.3 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 19
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon A., and Goldberg A.L. Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol. Cell 8 6 (2001) 1339-1349
    • (2001) Mol. Cell , vol.8 , Issue.6 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 20
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68 (1999) 1015-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 21
    • 0037449572 scopus 로고    scopus 로고
    • Endoproteolytic activity of the proteasome
    • Liu C.W., Corboy M.J., DeMartino G.N., and Thomas P.J. Endoproteolytic activity of the proteasome. Science 299 5605 (2003) 408-411
    • (2003) Science , vol.299 , Issue.5605 , pp. 408-411
    • Liu, C.W.1    Corboy, M.J.2    DeMartino, G.N.3    Thomas, P.J.4
  • 22
    • 0033529596 scopus 로고    scopus 로고
    • The proteasome, a novel protease regulated by multiple mechanisms
    • DeMartino G.N., and Slaughter C.A. The proteasome, a novel protease regulated by multiple mechanisms. J. Biol. Chem. 274 32 (1999) 22123-22126
    • (1999) J. Biol. Chem. , vol.274 , Issue.32 , pp. 22123-22126
    • DeMartino, G.N.1    Slaughter, C.A.2
  • 23
    • 13844280355 scopus 로고    scopus 로고
    • The axial channel of the 20S proteasome opens upon binding of the PA200 activator
    • Ortega J., Heymann J.B., Kajava A.V., Ustrell V., Rechsteiner M., and Steven A.C. The axial channel of the 20S proteasome opens upon binding of the PA200 activator. J. Mol. Biol. 346 5 (2005) 1221-1227
    • (2005) J. Mol. Biol. , vol.346 , Issue.5 , pp. 1221-1227
    • Ortega, J.1    Heymann, J.B.2    Kajava, A.V.3    Ustrell, V.4    Rechsteiner, M.5    Steven, A.C.6
  • 24
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors
    • Rechsteiner M., and Hill C.P. Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15 1 (2005) 27-33
    • (2005) Trends Cell Biol. , vol.15 , Issue.1 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 25
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O., Tanaka K., and Goldberg A.L. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65 (1996) 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 26
    • 33749234748 scopus 로고    scopus 로고
    • Proteasomes and their associated ATPases: a destructive combination
    • Smith D.M., Benaroudj N., and Goldberg A. Proteasomes and their associated ATPases: a destructive combination. J. Struct. Biol. 156 1 (2006) 72-83
    • (2006) J. Struct. Biol. , vol.156 , Issue.1 , pp. 72-83
    • Smith, D.M.1    Benaroudj, N.2    Goldberg, A.3
  • 27
    • 0037013955 scopus 로고    scopus 로고
    • Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes
    • Cascio P., Call M., Petre B.M., Walz T., and Goldberg A.L. Properties of the hybrid form of the 26S proteasome containing both 19S and PA28 complexes. EMBO J. 21 11 (2002) 2636-2645
    • (2002) EMBO J. , vol.21 , Issue.11 , pp. 2636-2645
    • Cascio, P.1    Call, M.2    Petre, B.M.3    Walz, T.4    Goldberg, A.L.5
  • 29
    • 0037401916 scopus 로고    scopus 로고
    • Intracellular localization of proteasomes
    • Wojcik C., and DeMartino G.N. Intracellular localization of proteasomes. Int. J. Biochem. Cell Biol. 35 5 (2003) 579-589
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , Issue.5 , pp. 579-589
    • Wojcik, C.1    DeMartino, G.N.2
  • 30
    • 44949169592 scopus 로고    scopus 로고
    • A novel role for PA28gamma-proteasome in nuclear speckle organization and SR protein trafficking
    • Baldin V., Militello M., Thomas Y., Doucet C., Fic W., Boireau S., et al. A novel role for PA28gamma-proteasome in nuclear speckle organization and SR protein trafficking. Mol. Biol. Cell 19 4 (2008) 1706-1716
    • (2008) Mol. Biol. Cell , vol.19 , Issue.4 , pp. 1706-1716
    • Baldin, V.1    Militello, M.2    Thomas, Y.3    Doucet, C.4    Fic, W.5    Boireau, S.6
  • 31
    • 0036260836 scopus 로고    scopus 로고
    • Brain proteasomal function in sporadic Parkinson's disease and related disorders
    • Furukawa Y., Vigouroux S., Wong H., Guttman M., Rajput A.H., Ang L., et al. Brain proteasomal function in sporadic Parkinson's disease and related disorders. Ann. Neurol. 51 6 (2002) 779-782
    • (2002) Ann. Neurol. , vol.51 , Issue.6 , pp. 779-782
    • Furukawa, Y.1    Vigouroux, S.2    Wong, H.3    Guttman, M.4    Rajput, A.H.5    Ang, L.6
  • 33
    • 0035910634 scopus 로고    scopus 로고
    • Proteasomal function is impaired in substantia nigra in Parkinson's disease
    • McNaught K.S., and Jenner P. Proteasomal function is impaired in substantia nigra in Parkinson's disease. Neurosci. Lett. 297 3 (2001) 191-194
    • (2001) Neurosci. Lett. , vol.297 , Issue.3 , pp. 191-194
    • McNaught, K.S.1    Jenner, P.2
  • 34
    • 0242666359 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function
    • Tofaris G.K., Razzaq A., Ghetti B., Lilley K.S., and Spillantini M.G. Ubiquitination of alpha-synuclein in Lewy bodies is a pathological event not associated with impairment of proteasome function. J. Biol. Chem. 278 45 (2003) 44405-44411
    • (2003) J. Biol. Chem. , vol.278 , Issue.45 , pp. 44405-44411
    • Tofaris, G.K.1    Razzaq, A.2    Ghetti, B.3    Lilley, K.S.4    Spillantini, M.G.5
  • 35
    • 0037025111 scopus 로고    scopus 로고
    • Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease
    • McNaught K.S., Belizaire R., Jenner P., Olanow C.W., and Isacson O. Selective loss of 20S proteasome alpha-subunits in the substantia nigra pars compacta in Parkinson's disease. Neurosci. Lett. 326 3 (2002) 155-158
    • (2002) Neurosci. Lett. , vol.326 , Issue.3 , pp. 155-158
    • McNaught, K.S.1    Belizaire, R.2    Jenner, P.3    Olanow, C.W.4    Isacson, O.5
  • 36
    • 0036468432 scopus 로고    scopus 로고
    • Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
    • Auluck P.K., Chan H.Y., Trojanowski J.Q., Lee V.M., and Bonini N.M. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease. Science 295 5556 (2002) 865-868
    • (2002) Science , vol.295 , Issue.5556 , pp. 865-868
    • Auluck, P.K.1    Chan, H.Y.2    Trojanowski, J.Q.3    Lee, V.M.4    Bonini, N.M.5
  • 37
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • Ii K., Ito H., Tanaka K., and Hirano A. Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 56 2 (1997) 125-131
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , Issue.2 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 38
    • 0024596151 scopus 로고
    • Anti-ubiquitin immunocytochemistry is more sensitive than conventional techniques in the detection of diffuse Lewy body disease
    • Lennox G., Lowe J., Morrell K., Landon M., and Mayer R.J. Anti-ubiquitin immunocytochemistry is more sensitive than conventional techniques in the detection of diffuse Lewy body disease. J. Neurol. Neurosurg. Psychiatry 52 1 (1989) 67-71
    • (1989) J. Neurol. Neurosurg. Psychiatry , vol.52 , Issue.1 , pp. 67-71
    • Lennox, G.1    Lowe, J.2    Morrell, K.3    Landon, M.4    Mayer, R.J.5
  • 39
    • 0025326719 scopus 로고
    • Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases
    • Lowe J., McDermott H., Landon M., Mayer R.J., and Wilkinson K.D. Ubiquitin carboxyl-terminal hydrolase (PGP 9.5) is selectively present in ubiquitinated inclusion bodies characteristic of human neurodegenerative diseases. J. Pathol. 161 2 (1990) 153-160
    • (1990) J. Pathol. , vol.161 , Issue.2 , pp. 153-160
    • Lowe, J.1    McDermott, H.2    Landon, M.3    Mayer, R.J.4    Wilkinson, K.D.5
  • 41
    • 0036095285 scopus 로고    scopus 로고
    • Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies
    • Schlossmacher M.G., Frosch M.P., Gai W.P., Medina M., Sharma N., Forno L., et al. Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies. Am. J. Pathol. 160 5 (2002) 1655-1667
    • (2002) Am. J. Pathol. , vol.160 , Issue.5 , pp. 1655-1667
    • Schlossmacher, M.G.1    Frosch, M.P.2    Gai, W.P.3    Medina, M.4    Sharma, N.5    Forno, L.6
  • 42
    • 0036316947 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures
    • McNaught K.S., Mytilineou C., Jnobaptiste R., Yabut J., Shashidharan P., Jennert P., et al. Impairment of the ubiquitin-proteasome system causes dopaminergic cell death and inclusion body formation in ventral mesencephalic cultures. J. Neurochem. 81 2 (2002) 301-306
    • (2002) J. Neurochem. , vol.81 , Issue.2 , pp. 301-306
    • McNaught, K.S.1    Mytilineou, C.2    Jnobaptiste, R.3    Yabut, J.4    Shashidharan, P.5    Jennert, P.6
  • 43
    • 20144381356 scopus 로고    scopus 로고
    • Dopaminergic neurons in rat ventral midbrain cultures undergo selective apoptosis and form inclusions, but do not up-regulate iHSP70, following proteasomal inhibition
    • Rideout H.J., Lang-Rollin I.C., Savalle M., and Stefanis L. Dopaminergic neurons in rat ventral midbrain cultures undergo selective apoptosis and form inclusions, but do not up-regulate iHSP70, following proteasomal inhibition. J. Neurochem. 93 5 (2005) 1304-1313
    • (2005) J. Neurochem. , vol.93 , Issue.5 , pp. 1304-1313
    • Rideout, H.J.1    Lang-Rollin, I.C.2    Savalle, M.3    Stefanis, L.4
  • 44
    • 3042794162 scopus 로고    scopus 로고
    • Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease
    • McNaught K.S., Perl D.P., Brownell A.L., and Olanow C.W. Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann. Neurol. 56 1 (2004) 149-162
    • (2004) Ann. Neurol. , vol.56 , Issue.1 , pp. 149-162
    • McNaught, K.S.1    Perl, D.P.2    Brownell, A.L.3    Olanow, C.W.4
  • 45
    • 33746839220 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced model of Parkinson's disease
    • McNaught K.S., and Olanow C.W. Proteasome inhibitor-induced model of Parkinson's disease. Ann. Neurol. 60 2 (2006) 243-247
    • (2006) Ann. Neurol. , vol.60 , Issue.2 , pp. 243-247
    • McNaught, K.S.1    Olanow, C.W.2
  • 47
    • 34548814747 scopus 로고    scopus 로고
    • Effects of systemic PSI administration on catecholaminergic cells in the brain, adrenal medulla and carotid body in Wistar rats
    • Hawlitschka A., Haas S.J., Schmitt O., Weiss D.G., and Wree A. Effects of systemic PSI administration on catecholaminergic cells in the brain, adrenal medulla and carotid body in Wistar rats. Brain Res. 1173 (2007) 137-144
    • (2007) Brain Res. , vol.1173 , pp. 137-144
    • Hawlitschka, A.1    Haas, S.J.2    Schmitt, O.3    Weiss, D.G.4    Wree, A.5
  • 48
    • 33746851988 scopus 로고    scopus 로고
    • Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys
    • Kordower J.H., Kanaan N.M., Chu Y., Suresh Babu R., Stansell III J., Terpstra B.T., et al. Failure of proteasome inhibitor administration to provide a model of Parkinson's disease in rats and monkeys. Ann. Neurol. 60 2 (2006) 264-268
    • (2006) Ann. Neurol. , vol.60 , Issue.2 , pp. 264-268
    • Kordower, J.H.1    Kanaan, N.M.2    Chu, Y.3    Suresh Babu, R.4    Stansell III, J.5    Terpstra, B.T.6
  • 51
    • 33746851548 scopus 로고    scopus 로고
    • Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats
    • Zeng B.Y., Bukhatwa S., Hikima A., Rose S., and Jenner P. Reproducible nigral cell loss after systemic proteasomal inhibitor administration to rats. Ann. Neurol. 60 2 (2006) 248-252
    • (2006) Ann. Neurol. , vol.60 , Issue.2 , pp. 248-252
    • Zeng, B.Y.1    Bukhatwa, S.2    Hikima, A.3    Rose, S.4    Jenner, P.5
  • 52
    • 51149121890 scopus 로고    scopus 로고
    • Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies
    • Bedford L., Hay D., Devoy A., Paine S., Powe D.G., Seth R., et al. Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J. Neurosci. 28 33 (2008) 8189-8198
    • (2008) J. Neurosci. , vol.28 , Issue.33 , pp. 8189-8198
    • Bedford, L.1    Hay, D.2    Devoy, A.3    Paine, S.4    Powe, D.G.5    Seth, R.6
  • 53
    • 33745612296 scopus 로고    scopus 로고
    • Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system
    • Betarbet R., Canet-Aviles R.M., Sherer T.B., Mastroberardino P.G., McLendon C., Kim J.H., et al. Intersecting pathways to neurodegeneration in Parkinson's disease: effects of the pesticide rotenone on DJ-1, alpha-synuclein, and the ubiquitin-proteasome system. Neurobiol. Dis. 22 2 (2006) 404-420
    • (2006) Neurobiol. Dis. , vol.22 , Issue.2 , pp. 404-420
    • Betarbet, R.1    Canet-Aviles, R.M.2    Sherer, T.B.3    Mastroberardino, P.G.4    McLendon, C.5    Kim, J.H.6
  • 54
    • 29644448325 scopus 로고    scopus 로고
    • Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function
    • Wang C., Ko H.S., Thomas B., Tsang F., Chew K.C., Tay S.P., et al. Stress-induced alterations in parkin solubility promote parkin aggregation and compromise parkin's protective function. Hum. Mol. Genet. 14 24 (2005) 3885-3897
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.24 , pp. 3885-3897
    • Wang, C.1    Ko, H.S.2    Thomas, B.3    Tsang, F.4    Chew, K.C.5    Tay, S.P.6
  • 55
    • 33745143950 scopus 로고    scopus 로고
    • Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease
    • Wang X.F., Li S., Chou A.P., and Bronstein J.M. Inhibitory effects of pesticides on proteasome activity: implication in Parkinson's disease. Neurobiol. Dis. 23 1 (2006) 198-205
    • (2006) Neurobiol. Dis. , vol.23 , Issue.1 , pp. 198-205
    • Wang, X.F.1    Li, S.2    Chou, A.P.3    Bronstein, J.M.4
  • 56
    • 20044385568 scopus 로고    scopus 로고
    • Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein
    • Fornai F., Schluter O.M., Lenzi P., Gesi M., Ruffoli R., Ferrucci M., et al. Parkinson-like syndrome induced by continuous MPTP infusion: convergent roles of the ubiquitin-proteasome system and alpha-synuclein. Proc. Natl. Acad. Sci. U. S. A. 102 9 (2005) 3413-3418
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.9 , pp. 3413-3418
    • Fornai, F.1    Schluter, O.M.2    Lenzi, P.3    Gesi, M.4    Ruffoli, R.5    Ferrucci, M.6
  • 57
    • 33645450436 scopus 로고    scopus 로고
    • MPTP treatment of common marmosets impairs proteasomal enzyme activity and decreases expression of structural and regulatory elements of the 26S proteasome
    • Zeng B.Y., Iravani M.M., Lin S.T., Irifune M., Kuoppamaki M., Al-Barghouthy G., et al. MPTP treatment of common marmosets impairs proteasomal enzyme activity and decreases expression of structural and regulatory elements of the 26S proteasome. Eur. J. Neurosci. 23 7 (2006) 1766-1774
    • (2006) Eur. J. Neurosci. , vol.23 , Issue.7 , pp. 1766-1774
    • Zeng, B.Y.1    Iravani, M.M.2    Lin, S.T.3    Irifune, M.4    Kuoppamaki, M.5    Al-Barghouthy, G.6
  • 60
    • 0023722437 scopus 로고
    • Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal
    • Maroteaux L., Campanelli J.T., and Scheller R.H. Synuclein: a neuron-specific protein localized to the nucleus and presynaptic nerve terminal. J. Neurosci. 8 8 (1988) 2804-2815
    • (1988) J. Neurosci. , vol.8 , Issue.8 , pp. 2804-2815
    • Maroteaux, L.1    Campanelli, J.T.2    Scheller, R.H.3
  • 61
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J. Biol. Chem. 273 16 (1998) 9443-9449
    • (1998) J. Biol. Chem. , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 62
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system
    • Abeliovich A., Schmitz Y., Farinas I., Choi-Lundberg D., Ho W.H., Castillo P.E., et al. Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system. Neuron 25 1 (2000) 239-252
    • (2000) Neuron , vol.25 , Issue.1 , pp. 239-252
    • Abeliovich, A.1    Schmitz, Y.2    Farinas, I.3    Choi-Lundberg, D.4    Ho, W.H.5    Castillo, P.E.6
  • 63
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein
    • Cabin D.E., Shimazu K., Murphy D., Cole N.B., Gottschalk W., McIlwain K.L., et al. Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking alpha-synuclein. J. Neurosci. 22 20 (2002) 8797-8807
    • (2002) J. Neurosci. , vol.22 , Issue.20 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6
  • 64
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • Murphy D.D., Rueter S.M., Trojanowski J.Q., and Lee V.M. Synucleins are developmentally expressed, and alpha-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons. J. Neurosci. 20 9 (2000) 3214-3220
    • (2000) J. Neurosci. , vol.20 , Issue.9 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 65
    • 33750041624 scopus 로고    scopus 로고
    • Abnormal compartmentalization of norepinephrine in mouse dentate gyrus in alpha-synuclein knockout and A30P transgenic mice
    • Yavich L., Jakala P., and Tanila H. Abnormal compartmentalization of norepinephrine in mouse dentate gyrus in alpha-synuclein knockout and A30P transgenic mice. J. Neurochem. 99 3 (2006) 724-732
    • (2006) J. Neurochem. , vol.99 , Issue.3 , pp. 724-732
    • Yavich, L.1    Jakala, P.2    Tanila, H.3
  • 66
    • 10944243102 scopus 로고    scopus 로고
    • Role of alpha-synuclein in presynaptic dopamine recruitment
    • Yavich L., Tanila H., Vepsalainen S., and Jakala P. Role of alpha-synuclein in presynaptic dopamine recruitment. J. Neurosci. 24 49 (2004) 11165-11170
    • (2004) J. Neurosci. , vol.24 , Issue.49 , pp. 11165-11170
    • Yavich, L.1    Tanila, H.2    Vepsalainen, S.3    Jakala, P.4
  • 69
    • 51049113435 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor-tropomyosin-related kinase B signaling contributes to activity-dependent changes in synaptic proteins
    • Jia J.M., Chen Q., Zhou Y., Miao S., Zheng J., Zhang C., et al. Brain-derived neurotrophic factor-tropomyosin-related kinase B signaling contributes to activity-dependent changes in synaptic proteins. J. Biol. Chem. 283 30 (2008) 21242-21250
    • (2008) J. Biol. Chem. , vol.283 , Issue.30 , pp. 21242-21250
    • Jia, J.M.1    Chen, Q.2    Zhou, Y.3    Miao, S.4    Zheng, J.5    Zhang, C.6
  • 70
    • 0028829061 scopus 로고
    • Monocular deprivation decreases the expression of messenger RNA for brain-derived neurotrophic factor in the rat visual cortex
    • Bozzi Y., Pizzorusso T., Cremisi F., Rossi F.M., Barsacchi G., and Maffei L. Monocular deprivation decreases the expression of messenger RNA for brain-derived neurotrophic factor in the rat visual cortex. Neuroscience 69 4 (1995) 1133-1144
    • (1995) Neuroscience , vol.69 , Issue.4 , pp. 1133-1144
    • Bozzi, Y.1    Pizzorusso, T.2    Cremisi, F.3    Rossi, F.M.4    Barsacchi, G.5    Maffei, L.6
  • 71
    • 0036241207 scopus 로고    scopus 로고
    • Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways
    • Hardingham G.E., Fukunaga Y., and Bading H. Extrasynaptic NMDARs oppose synaptic NMDARs by triggering CREB shut-off and cell death pathways. Nat. Neurosci. 5 5 (2002) 405-414
    • (2002) Nat. Neurosci. , vol.5 , Issue.5 , pp. 405-414
    • Hardingham, G.E.1    Fukunaga, Y.2    Bading, H.3
  • 72
    • 0025883295 scopus 로고
    • BDNF mRNA expression is increased in adult rat forebrain after limbic seizures: temporal patterns of induction distinct from NGF
    • Isackson P.J., Huntsman M.M., Murray K.D., and Gall C.M. BDNF mRNA expression is increased in adult rat forebrain after limbic seizures: temporal patterns of induction distinct from NGF. Neuron 6 6 (1991) 937-948
    • (1991) Neuron , vol.6 , Issue.6 , pp. 937-948
    • Isackson, P.J.1    Huntsman, M.M.2    Murray, K.D.3    Gall, C.M.4
  • 73
    • 0025889012 scopus 로고
    • Interplay between glutamate and gamma-aminobutyric acid transmitter systems in the physiological regulation of brain-derived neurotrophic factor and nerve growth factor synthesis in hippocampal neurons
    • Zafra F., Castren E., Thoenen H., and Lindholm D. Interplay between glutamate and gamma-aminobutyric acid transmitter systems in the physiological regulation of brain-derived neurotrophic factor and nerve growth factor synthesis in hippocampal neurons. Proc. Natl. Acad. Sci. U. S. A. 88 22 (1991) 10037-10041
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , Issue.22 , pp. 10037-10041
    • Zafra, F.1    Castren, E.2    Thoenen, H.3    Lindholm, D.4
  • 74
    • 0037016741 scopus 로고    scopus 로고
    • Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form
    • Lee H.J., Choi C., and Lee S.J. Membrane-bound alpha-synuclein has a high aggregation propensity and the ability to seed the aggregation of the cytosolic form. J. Biol. Chem. 277 1 (2002) 671-678
    • (2002) J. Biol. Chem. , vol.277 , Issue.1 , pp. 671-678
    • Lee, H.J.1    Choi, C.2    Lee, S.J.3
  • 75
    • 4344585351 scopus 로고    scopus 로고
    • Age-related changes in nigrostriatal dopaminergic function are accentuated in +/- brain-derived neurotrophic factor mice
    • Dluzen D.E., McDermott J.L., Anderson L.I., Kucera J., Joyce J.N., Osredkar T., et al. Age-related changes in nigrostriatal dopaminergic function are accentuated in +/- brain-derived neurotrophic factor mice. Neuroscience 128 1 (2004) 201-208
    • (2004) Neuroscience , vol.128 , Issue.1 , pp. 201-208
    • Dluzen, D.E.1    McDermott, J.L.2    Anderson, L.I.3    Kucera, J.4    Joyce, J.N.5    Osredkar, T.6
  • 76
    • 17844406856 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease
    • Chen L., and Feany M.B. Alpha-synuclein phosphorylation controls neurotoxicity and inclusion formation in a Drosophila model of Parkinson disease. Nat. Neurosci. 8 5 (2005) 657-663
    • (2005) Nat. Neurosci. , vol.8 , Issue.5 , pp. 657-663
    • Chen, L.1    Feany, M.B.2
  • 78
    • 0034602442 scopus 로고    scopus 로고
    • Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions
    • Giasson B.I., Duda J.E., Murray I.V., Chen Q., Souza J.M., Hurtig H.I., et al. Oxidative damage linked to neurodegeneration by selective alpha-synuclein nitration in synucleinopathy lesions. Science 290 5493 (2000) 985-989
    • (2000) Science , vol.290 , Issue.5493 , pp. 985-989
    • Giasson, B.I.1    Duda, J.E.2    Murray, I.V.3    Chen, Q.4    Souza, J.M.5    Hurtig, H.I.6
  • 80
    • 0033583215 scopus 로고    scopus 로고
    • Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro
    • Giasson B.I., Uryu K., Trojanowski J.Q., and Lee V.M. Mutant and wild type human alpha-synucleins assemble into elongated filaments with distinct morphologies in vitro. J. Biol. Chem. 274 12 (1999) 7619-7622
    • (1999) J. Biol. Chem. , vol.274 , Issue.12 , pp. 7619-7622
    • Giasson, B.I.1    Uryu, K.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 81
    • 9144229591 scopus 로고    scopus 로고
    • Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation
    • Hodara R., Norris E.H., Giasson B.I., Mishizen-Eberz A.J., Lynch D.R., Lee V.M., et al. Functional consequences of alpha-synuclein tyrosine nitration: diminished binding to lipid vesicles and increased fibril formation. J. Biol. Chem. 279 46 (2004) 47746-47753
    • (2004) J. Biol. Chem. , vol.279 , Issue.46 , pp. 47746-47753
    • Hodara, R.1    Norris, E.H.2    Giasson, B.I.3    Mishizen-Eberz, A.J.4    Lynch, D.R.5    Lee, V.M.6
  • 82
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • Li W., West N., Colla E., Pletnikova O., Troncoso J.C., Marsh L., et al. Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc. Natl. Acad. Sci. U. S. A. 102 6 (2005) 2162-2167
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.6 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6
  • 83
    • 19644371237 scopus 로고    scopus 로고
    • Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein
    • Mishizen-Eberz A.J., Norris E.H., Giasson B.I., Hodara R., Ischiropoulos H., Lee V.M., et al. Cleavage of alpha-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of alpha-synuclein. Biochemistry 44 21 (2005) 7818-7829
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7818-7829
    • Mishizen-Eberz, A.J.1    Norris, E.H.2    Giasson, B.I.3    Hodara, R.4    Ischiropoulos, H.5    Lee, V.M.6
  • 85
    • 0038711511 scopus 로고    scopus 로고
    • Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications
    • Norris E.H., Giasson B.I., Ischiropoulos H., and Lee V.M. Effects of oxidative and nitrative challenges on alpha-synuclein fibrillogenesis involve distinct mechanisms of protein modifications. J. Biol. Chem. 278 29 (2003) 27230-27240
    • (2003) J. Biol. Chem. , vol.278 , Issue.29 , pp. 27230-27240
    • Norris, E.H.1    Giasson, B.I.2    Ischiropoulos, H.3    Lee, V.M.4
  • 86
    • 4644295844 scopus 로고    scopus 로고
    • Parkinson's disease and dementia with Lewy bodies: a difference in dose?
    • Singleton A., and Gwinn-Hardy K. Parkinson's disease and dementia with Lewy bodies: a difference in dose?. Lancet 364 9440 (2004) 1105-1107
    • (2004) Lancet , vol.364 , Issue.9440 , pp. 1105-1107
    • Singleton, A.1    Gwinn-Hardy, K.2
  • 87
    • 20444416315 scopus 로고    scopus 로고
    • Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells
    • Smith W.W., Margolis R.L., Li X., Troncoso J.C., Lee M.K., Dawson V.L., et al. Alpha-synuclein phosphorylation enhances eosinophilic cytoplasmic inclusion formation in SH-SY5Y cells. J. Neurosci. 25 23 (2005) 5544-5552
    • (2005) J. Neurosci. , vol.25 , Issue.23 , pp. 5544-5552
    • Smith, W.W.1    Margolis, R.L.2    Li, X.3    Troncoso, J.C.4    Lee, M.K.5    Dawson, V.L.6
  • 88
    • 33646097224 scopus 로고    scopus 로고
    • Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1-120): implications for Lewy body disorders
    • Tofaris G.K., Garcia Reitbock P., Humby T., Lambourne S.L., O'Connell M., Ghetti B., et al. Pathological changes in dopaminergic nerve cells of the substantia nigra and olfactory bulb in mice transgenic for truncated human alpha-synuclein(1-120): implications for Lewy body disorders. J. Neurosci. 26 15 (2006) 3942-3950
    • (2006) J. Neurosci. , vol.26 , Issue.15 , pp. 3942-3950
    • Tofaris, G.K.1    Garcia Reitbock, P.2    Humby, T.3    Lambourne, S.L.4    O'Connell, M.5    Ghetti, B.6
  • 89
    • 20444401187 scopus 로고    scopus 로고
    • Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations
    • Norris E.H., Giasson B.I., Hodara R., Xu S., Trojanowski J.Q., Ischiropoulos H., et al. Reversible inhibition of alpha-synuclein fibrillization by dopaminochrome-mediated conformational alterations. J. Biol. Chem. 280 22 (2005) 21212-21219
    • (2005) J. Biol. Chem. , vol.280 , Issue.22 , pp. 21212-21219
    • Norris, E.H.1    Giasson, B.I.2    Hodara, R.3    Xu, S.4    Trojanowski, J.Q.5    Ischiropoulos, H.6
  • 90
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation
    • Serpell L.C., Berriman J., Jakes R., Goedert M., and Crowther R.A. Fiber diffraction of synthetic alpha-synuclein filaments shows amyloid-like cross-beta conformation. Proc. Natl. Acad. Sci. U. S. A. 97 9 (2000) 4897-4902
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.9 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 91
    • 0033577159 scopus 로고    scopus 로고
    • Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro
    • Hashimoto M., Hsu L.J., Xia Y., Takeda A., Sisk A., Sundsmo M., et al. Oxidative stress induces amyloid-like aggregate formation of NACP/alpha-synuclein in vitro. NeuroReport 10 4 (1999) 717-721
    • (1999) NeuroReport , vol.10 , Issue.4 , pp. 717-721
    • Hashimoto, M.1    Hsu, L.J.2    Xia, Y.3    Takeda, A.4    Sisk, A.5    Sundsmo, M.6
  • 92
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson J.P., Walker D.E., Goldstein J.M., de Laat R., Banducci K., Caccavello R.J., et al. Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J. Biol. Chem. 281 40 (2006) 29739-29752
    • (2006) J. Biol. Chem. , vol.281 , Issue.40 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3    de Laat, R.4    Banducci, K.5    Caccavello, R.J.6
  • 93
    • 43249108653 scopus 로고    scopus 로고
    • Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein
    • Waxman E.A., and Giasson B.I. Specificity and regulation of casein kinase-mediated phosphorylation of alpha-synuclein. J. Neuropathol. Exp. Neurol. 67 5 (2008) 402-416
    • (2008) J. Neuropathol. Exp. Neurol. , vol.67 , Issue.5 , pp. 402-416
    • Waxman, E.A.1    Giasson, B.I.2
  • 94
    • 33748483511 scopus 로고    scopus 로고
    • The role of G-protein-coupled receptor kinase 5 in pathogenesis of sporadic Parkinson's disease
    • Arawaka S., Wada M., Goto S., Karube H., Sakamoto M., Ren C.H., et al. The role of G-protein-coupled receptor kinase 5 in pathogenesis of sporadic Parkinson's disease. J. Neurosci. 26 36 (2006) 9227-9238
    • (2006) J. Neurosci. , vol.26 , Issue.36 , pp. 9227-9238
    • Arawaka, S.1    Wada, M.2    Goto, S.3    Karube, H.4    Sakamoto, M.5    Ren, C.H.6
  • 95
    • 0034614415 scopus 로고    scopus 로고
    • Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein
    • Okochi M., Walter J., Koyama A., Nakajo S., Baba M., Iwatsubo T., et al. Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. J. Biol. Chem. 275 1 (2000) 390-397
    • (2000) J. Biol. Chem. , vol.275 , Issue.1 , pp. 390-397
    • Okochi, M.1    Walter, J.2    Koyama, A.3    Nakajo, S.4    Baba, M.5    Iwatsubo, T.6
  • 96
    • 47749107973 scopus 로고    scopus 로고
    • Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein
    • Paleologou K.E., Schmid A.W., Rospigliosi C.C., Kim H.Y., Lamberto G.R., Fredenburg R.A., et al. Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein. J. Biol. Chem. 283 24 (2008) 16895-16905
    • (2008) J. Biol. Chem. , vol.283 , Issue.24 , pp. 16895-16905
    • Paleologou, K.E.1    Schmid, A.W.2    Rospigliosi, C.C.3    Kim, H.Y.4    Lamberto, G.R.5    Fredenburg, R.A.6
  • 97
    • 0034714204 scopus 로고    scopus 로고
    • Synucleins are a novel class of substrates for G protein-coupled receptor kinases
    • Pronin A.N., Morris A.J., Surguchov A., and Benovic J.L. Synucleins are a novel class of substrates for G protein-coupled receptor kinases. J. Biol. Chem. 275 34 (2000) 26515-26522
    • (2000) J. Biol. Chem. , vol.275 , Issue.34 , pp. 26515-26522
    • Pronin, A.N.1    Morris, A.J.2    Surguchov, A.3    Benovic, J.L.4
  • 98
    • 34347260686 scopus 로고    scopus 로고
    • Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis
    • Liu C., Fei E., Jia N., Wang H., Tao R., Iwata A., et al. Assembly of lysine 63-linked ubiquitin conjugates by phosphorylated alpha-synuclein implies Lewy body biogenesis. J. Biol. Chem. 282 19 (2007) 14558-14566
    • (2007) J. Biol. Chem. , vol.282 , Issue.19 , pp. 14558-14566
    • Liu, C.1    Fei, E.2    Jia, N.3    Wang, H.4    Tao, R.5    Iwata, A.6
  • 99
    • 53149133169 scopus 로고    scopus 로고
    • Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediated cell death
    • Sugeno N., Takeda A., Hasegawa T., Kobayashi M., Kikuchi A., Mori F., et al. Serine 129 phosphorylation of alpha-synuclein induces unfolded protein response-mediated cell death. J. Biol. Chem. 283 34 (2008) 23179-23188
    • (2008) J. Biol. Chem. , vol.283 , Issue.34 , pp. 23179-23188
    • Sugeno, N.1    Takeda, A.2    Hasegawa, T.3    Kobayashi, M.4    Kikuchi, A.5    Mori, F.6
  • 100
    • 38649084032 scopus 로고    scopus 로고
    • The phosphorylation state of Ser-129 in human alpha-synuclein determines neurodegeneration in a rat model of Parkinson disease
    • Gorbatyuk O.S., Li S., Sullivan L.F., Chen W., Kondrikova G., Manfredsson F.P., et al. The phosphorylation state of Ser-129 in human alpha-synuclein determines neurodegeneration in a rat model of Parkinson disease. Proc. Natl. Acad. Sci. U. S. A. 105 2 (2008) 763-768
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , Issue.2 , pp. 763-768
    • Gorbatyuk, O.S.1    Li, S.2    Sullivan, L.F.3    Chen, W.4    Kondrikova, G.5    Manfredsson, F.P.6
  • 101
    • 40549090917 scopus 로고    scopus 로고
    • Ubiquitination of alpha-synuclein by Siah-1 promotes alpha-synuclein aggregation and apoptotic cell death
    • Lee J.T., Wheeler T.C., Li L., and Chin L.S. Ubiquitination of alpha-synuclein by Siah-1 promotes alpha-synuclein aggregation and apoptotic cell death. Hum. Mol. Genet. 17 6 (2008) 906-917
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.6 , pp. 906-917
    • Lee, J.T.1    Wheeler, T.C.2    Li, L.3    Chin, L.S.4
  • 102
    • 41249090880 scopus 로고    scopus 로고
    • Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells
    • Rott R., Szargel R., Haskin J., Shani V., Shainskaya A., Manov I., et al. Monoubiquitylation of alpha-synuclein by seven in absentia homolog (SIAH) promotes its aggregation in dopaminergic cells. J. Biol. Chem. 283 6 (2008) 3316-3328
    • (2008) J. Biol. Chem. , vol.283 , Issue.6 , pp. 3316-3328
    • Rott, R.1    Szargel, R.2    Haskin, J.3    Shani, V.4    Shainskaya, A.5    Manov, I.6
  • 103
    • 0036797038 scopus 로고    scopus 로고
    • Synphilin-1 degradation by the ubiquitin-proteasome pathway and effects on cell survival
    • Lee G., Junn E., Tanaka M., Kim Y.M., and Mouradian M.M. Synphilin-1 degradation by the ubiquitin-proteasome pathway and effects on cell survival. J. Neurochem. 83 2 (2002) 346-352
    • (2002) J. Neurochem. , vol.83 , Issue.2 , pp. 346-352
    • Lee, G.1    Junn, E.2    Tanaka, M.3    Kim, Y.M.4    Mouradian, M.M.5
  • 104
    • 11144358336 scopus 로고    scopus 로고
    • Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease
    • Liani E., Eyal A., Avraham E., Shemer R., Szargel R., Berg D., et al. Ubiquitylation of synphilin-1 and alpha-synuclein by SIAH and its presence in cellular inclusions and Lewy bodies imply a role in Parkinson's disease. Proc. Natl. Acad. Sci. U. S. A. 101 15 (2004) 5500-5505
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , Issue.15 , pp. 5500-5505
    • Liani, E.1    Eyal, A.2    Avraham, E.3    Shemer, R.4    Szargel, R.5    Berg, D.6
  • 105
    • 34249803290 scopus 로고    scopus 로고
    • The proteasomal subunit S6 ATPase is a novel synphilin-1 interacting protein-implications for Parkinson's disease
    • Marx F.P., Soehn A.S., Berg D., Melle C., Schiesling C., Lang M., et al. The proteasomal subunit S6 ATPase is a novel synphilin-1 interacting protein-implications for Parkinson's disease. Faseb. J. 21 8 (2007) 1759-1767
    • (2007) Faseb. J. , vol.21 , Issue.8 , pp. 1759-1767
    • Marx, F.P.1    Soehn, A.S.2    Berg, D.3    Melle, C.4    Schiesling, C.5    Lang, M.6
  • 106
    • 30044440010 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation
    • Avraham E., Szargel R., Eyal A., Rott R., and Engelender S. Glycogen synthase kinase 3beta modulates synphilin-1 ubiquitylation and cellular inclusion formation by SIAH: implications for proteasomal function and Lewy body formation. J. Biol. Chem. 280 52 (2005) 42877-42886
    • (2005) J. Biol. Chem. , vol.280 , Issue.52 , pp. 42877-42886
    • Avraham, E.1    Szargel, R.2    Eyal, A.3    Rott, R.4    Engelender, S.5
  • 107
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • Baba M., Nakajo S., Tu P.H., Tomita T., Nakaya K., Lee V.M., et al. Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am. J. Pathol. 152 4 (1998) 879-884
    • (1998) Am. J. Pathol. , vol.152 , Issue.4 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6
  • 108
    • 0035163412 scopus 로고    scopus 로고
    • The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease
    • Campbell B.C., McLean C.A., Culvenor J.G., Gai W.P., Blumbergs P.C., Jakala P., et al. The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease. J. Neurochem. 76 1 (2001) 87-96
    • (2001) J. Neurochem. , vol.76 , Issue.1 , pp. 87-96
    • Campbell, B.C.1    McLean, C.A.2    Culvenor, J.G.3    Gai, W.P.4    Blumbergs, P.C.5    Jakala, P.6
  • 109
    • 0031728689 scopus 로고    scopus 로고
    • Synthetic filaments assembled from C-terminally truncated alpha-synuclein
    • Crowther R.A., Jakes R., Spillantini M.G., and Goedert M. Synthetic filaments assembled from C-terminally truncated alpha-synuclein. FEBS Lett. 436 3 (1998) 309-312
    • (1998) FEBS Lett. , vol.436 , Issue.3 , pp. 309-312
    • Crowther, R.A.1    Jakes, R.2    Spillantini, M.G.3    Goedert, M.4
  • 110
    • 23444455247 scopus 로고    scopus 로고
    • Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway
    • Cappai R., Leck S.L., Tew D.J., Williamson N.A., Smith D.P., Galatis D., et al. Dopamine promotes alpha-synuclein aggregation into SDS-resistant soluble oligomers via a distinct folding pathway. FASEB J. 19 10 (2005) 1377-1379
    • (2005) FASEB J. , vol.19 , Issue.10 , pp. 1377-1379
    • Cappai, R.1    Leck, S.L.2    Tew, D.J.3    Williamson, N.A.4    Smith, D.P.5    Galatis, D.6
  • 111
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway K.A., Rochet J.C., Bieganski R.M., and Lansbury Jr. P.T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294 5545 (2001) 1346-1349
    • (2001) Science , vol.294 , Issue.5545 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury Jr., P.T.4
  • 112
    • 4344650564 scopus 로고    scopus 로고
    • Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease
    • Li J., Zhu M., Manning-Bog A.B., Di Monte D.A., and Fink A.L. Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease. FASEB J. 18 9 (2004) 962-964
    • (2004) FASEB J. , vol.18 , Issue.9 , pp. 962-964
    • Li, J.1    Zhu, M.2    Manning-Bog, A.B.3    Di Monte, D.A.4    Fink, A.L.5
  • 113
    • 0036278335 scopus 로고    scopus 로고
    • Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease
    • Xu J., Kao S.Y., Lee F.J., Song W., Jin L.W., and Yankner B.A. Dopamine-dependent neurotoxicity of alpha-synuclein: a mechanism for selective neurodegeneration in Parkinson disease. Nat. Med. 8 6 (2002) 600-606
    • (2002) Nat. Med. , vol.8 , Issue.6 , pp. 600-606
    • Xu, J.1    Kao, S.Y.2    Lee, F.J.3    Song, W.4    Jin, L.W.5    Yankner, B.A.6
  • 114
    • 33749170166 scopus 로고    scopus 로고
    • Cytosolic catechols inhibit alpha-synuclein aggregation and facilitate the formation of intracellular soluble oligomeric intermediates
    • Mazzulli J.R., Mishizen A.J., Giasson B.I., Lynch D.R., Thomas S.A., Nakashima A., et al. Cytosolic catechols inhibit alpha-synuclein aggregation and facilitate the formation of intracellular soluble oligomeric intermediates. J. Neurosci. 26 39 (2006) 10068-10078
    • (2006) J. Neurosci. , vol.26 , Issue.39 , pp. 10068-10078
    • Mazzulli, J.R.1    Mishizen, A.J.2    Giasson, B.I.3    Lynch, D.R.4    Thomas, S.A.5    Nakashima, A.6
  • 115
    • 35748975424 scopus 로고    scopus 로고
    • Cellular oligomerization of alpha-synuclein is determined by the interaction of oxidized catechols with a C-terminal sequence
    • Mazzulli J.R., Armakola M., Dumoulin M., Parastatidis I., and Ischiropoulos H. Cellular oligomerization of alpha-synuclein is determined by the interaction of oxidized catechols with a C-terminal sequence. J. Biol. Chem. 282 43 (2007) 31621-31630
    • (2007) J. Biol. Chem. , vol.282 , Issue.43 , pp. 31621-31630
    • Mazzulli, J.R.1    Armakola, M.2    Dumoulin, M.3    Parastatidis, I.4    Ischiropoulos, H.5
  • 117
    • 0034640160 scopus 로고    scopus 로고
    • Alpha-synuclein and the Parkinson's disease-related mutant Ala53Thr-alpha-synuclein do not undergo proteasomal degradation in HEK293 and neuronal cells
    • Ancolio K., Alves da Costa C., Ueda K., and Checler F. Alpha-synuclein and the Parkinson's disease-related mutant Ala53Thr-alpha-synuclein do not undergo proteasomal degradation in HEK293 and neuronal cells. Neurosci. Lett. 285 2 (2000) 79-82
    • (2000) Neurosci. Lett. , vol.285 , Issue.2 , pp. 79-82
    • Ancolio, K.1    Alves da Costa, C.2    Ueda, K.3    Checler, F.4
  • 118
    • 34250832784 scopus 로고    scopus 로고
    • Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation
    • Dufty B.M., Warner L.R., Hou S.T., Jiang S.X., Gomez-Isla T., Leenhouts K.M., et al. Calpain-cleavage of alpha-synuclein: connecting proteolytic processing to disease-linked aggregation. Am. J. Pathol. 170 5 (2007) 1725-1738
    • (2007) Am. J. Pathol. , vol.170 , Issue.5 , pp. 1725-1738
    • Dufty, B.M.1    Warner, L.R.2    Hou, S.T.3    Jiang, S.X.4    Gomez-Isla, T.5    Leenhouts, K.M.6
  • 119
    • 33750151957 scopus 로고    scopus 로고
    • Calpain-resistant fragment(s) of alpha-synuclein regulates the synuclein-cleaving activity of 20S proteasome
    • Kim H.J., Lee D., Lee C.H., Chung K.C., Kim J., and Paik S.R. Calpain-resistant fragment(s) of alpha-synuclein regulates the synuclein-cleaving activity of 20S proteasome. Arch. Biochem. Biophys. 455 1 (2006) 40-47
    • (2006) Arch. Biochem. Biophys. , vol.455 , Issue.1 , pp. 40-47
    • Kim, H.J.1    Lee, D.2    Lee, C.H.3    Chung, K.C.4    Kim, J.5    Paik, S.R.6
  • 120
    • 15744402739 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments
    • Cole N.B., Murphy D.D., Lebowitz J., Di Noto L., Levine R.L., and Nussbaum R.L. Metal-catalyzed oxidation of alpha-synuclein: helping to define the relationship between oligomers, protofibrils, and filaments. J. Biol. Chem. 280 10 (2005) 9678-9690
    • (2005) J. Biol. Chem. , vol.280 , Issue.10 , pp. 9678-9690
    • Cole, N.B.1    Murphy, D.D.2    Lebowitz, J.3    Di Noto, L.4    Levine, R.L.5    Nussbaum, R.L.6
  • 121
    • 0035976835 scopus 로고    scopus 로고
    • alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome
    • Tofaris G.K., Layfield R., and Spillantini M.G. alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett. 509 1 (2001) 22-26
    • (2001) FEBS Lett. , vol.509 , Issue.1 , pp. 22-26
    • Tofaris, G.K.1    Layfield, R.2    Spillantini, M.G.3
  • 122
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease
    • Liu C.W., Giasson B.I., Lewis K.A., Lee V.M., Demartino G.N., and Thomas P.J. A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: implications for pathogenesis of Parkinson disease. J. Biol. Chem. 280 24 (2005) 22670-22678
    • (2005) J. Biol. Chem. , vol.280 , Issue.24 , pp. 22670-22678
    • Liu, C.W.1    Giasson, B.I.2    Lewis, K.A.3    Lee, V.M.4    Demartino, G.N.5    Thomas, P.J.6
  • 123
    • 0032500599 scopus 로고    scopus 로고
    • Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation
    • Jensen P.H., Nielsen M.S., Jakes R., Dotti C.G., and Goedert M. Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation. J. Biol. Chem. 273 41 (1998) 26292-26294
    • (1998) J. Biol. Chem. , vol.273 , Issue.41 , pp. 26292-26294
    • Jensen, P.H.1    Nielsen, M.S.2    Jakes, R.3    Dotti, C.G.4    Goedert, M.5
  • 124
    • 3142514196 scopus 로고    scopus 로고
    • Oxidative stress in neurodegeneration: cause or consequence?
    • Andersen J.K. Oxidative stress in neurodegeneration: cause or consequence?. Nat. Med. 10 Suppl (2004) S18-25
    • (2004) Nat. Med. , vol.10 SUPPL
    • Andersen, J.K.1
  • 125
    • 0035870881 scopus 로고    scopus 로고
    • Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis
    • Tanaka Y., Engelender S., Igarashi S., Rao R.K., Wanner T., Tanzi R.E., et al. Inducible expression of mutant alpha-synuclein decreases proteasome activity and increases sensitivity to mitochondria-dependent apoptosis. Hum. Mol. Genet. 10 9 (2001) 919-926
    • (2001) Hum. Mol. Genet. , vol.10 , Issue.9 , pp. 919-926
    • Tanaka, Y.1    Engelender, S.2    Igarashi, S.3    Rao, R.K.4    Wanner, T.5    Tanzi, R.E.6
  • 126
    • 19944407418 scopus 로고    scopus 로고
    • alpha-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines
    • Martin-Clemente B., Alvarez-Castelao B., Mayo I., Sierra A.B., Diaz V., Milan M., et al. alpha-Synuclein expression levels do not significantly affect proteasome function and expression in mice and stably transfected PC12 cell lines. J. Biol. Chem. 279 51 (2004) 52984-52990
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 52984-52990
    • Martin-Clemente, B.1    Alvarez-Castelao, B.2    Mayo, I.3    Sierra, A.B.4    Diaz, V.5    Milan, M.6
  • 127
    • 34247177526 scopus 로고    scopus 로고
    • alpha-Synuclein stimulates differentiation of osteosarcoma cells: relevance to down-regulation of proteasome activity
    • Fujita M., Sugama S., Nakai M., Takenouchi T., Wei J., Urano T., et al. alpha-Synuclein stimulates differentiation of osteosarcoma cells: relevance to down-regulation of proteasome activity. J. Biol. Chem. 282 8 (2007) 5736-5748
    • (2007) J. Biol. Chem. , vol.282 , Issue.8 , pp. 5736-5748
    • Fujita, M.1    Sugama, S.2    Nakai, M.3    Takenouchi, T.4    Wei, J.5    Urano, T.6
  • 128
    • 25644446864 scopus 로고    scopus 로고
    • Dieldrin induces ubiquitin-proteasome dysfunction in alpha-synuclein overexpressing dopaminergic neuronal cells and enhances susceptibility to apoptotic cell death
    • Sun F., Anantharam V., Latchoumycandane C., Kanthasamy A., and Kanthasamy A.G. Dieldrin induces ubiquitin-proteasome dysfunction in alpha-synuclein overexpressing dopaminergic neuronal cells and enhances susceptibility to apoptotic cell death. J. Pharmacol. Exp. Ther. 315 1 (2005) 69-79
    • (2005) J. Pharmacol. Exp. Ther. , vol.315 , Issue.1 , pp. 69-79
    • Sun, F.1    Anantharam, V.2    Latchoumycandane, C.3    Kanthasamy, A.4    Kanthasamy, A.G.5
  • 129
    • 33645235438 scopus 로고    scopus 로고
    • Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases
    • Bodner R.A., Outeiro T.F., Altmann S., Maxwell M.M., Cho S.H., Hyman B.T., et al. Pharmacological promotion of inclusion formation: a therapeutic approach for Huntington's and Parkinson's diseases. Proc. Natl. Acad. Sci. U. S. A. 103 11 (2006) 4246-4251
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.11 , pp. 4246-4251
    • Bodner, R.A.1    Outeiro, T.F.2    Altmann, S.3    Maxwell, M.M.4    Cho, S.H.5    Hyman, B.T.6
  • 130
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli L., O'Farrell C., Lockhart P.J., Baptista M., Kehoe K., Vink L., et al. Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 36 6 (2002) 1007-1019
    • (2002) Neuron , vol.36 , Issue.6 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6
  • 131
    • 24044516868 scopus 로고    scopus 로고
    • Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability
    • Chen Q., Thorpe J., and Keller J.N. Alpha-synuclein alters proteasome function, protein synthesis, and stationary phase viability. J. Biol. Chem. 280 34 (2005) 30009-30017
    • (2005) J. Biol. Chem. , vol.280 , Issue.34 , pp. 30009-30017
    • Chen, Q.1    Thorpe, J.2    Keller, J.N.3
  • 132
    • 39749185957 scopus 로고    scopus 로고
    • A molecular pathway of neurodegeneration linking alpha-synuclein to ApoE and Abeta peptides
    • Gallardo G., Schluter O.M., and Sudhof T.C. A molecular pathway of neurodegeneration linking alpha-synuclein to ApoE and Abeta peptides. Nat. Neurosci. 11 3 (2008) 301-308
    • (2008) Nat. Neurosci. , vol.11 , Issue.3 , pp. 301-308
    • Gallardo, G.1    Schluter, O.M.2    Sudhof, T.C.3
  • 133
    • 53549111497 scopus 로고    scopus 로고
    • Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome
    • Emmanouilidou E., Stefanis L., and Vekrellis K. Cell-produced alpha-synuclein oligomers are targeted to, and impair, the 26S proteasome. Neurobiol. Aging (2008)
    • (2008) Neurobiol. Aging
    • Emmanouilidou, E.1    Stefanis, L.2    Vekrellis, K.3
  • 134
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by alpha-synuclein filaments and oligomers
    • Lindersson E., Beedholm R., Hojrup P., Moos T., Gai W., Hendil K.B., et al. Proteasomal inhibition by alpha-synuclein filaments and oligomers. J. Biol. Chem. 279 13 (2004) 12924-12934
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3    Moos, T.4    Gai, W.5    Hendil, K.B.6
  • 135
    • 0038413759 scopus 로고    scopus 로고
    • Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function
    • Snyder H., Mensah K., Theisler C., Lee J., Matouschek A., and Wolozin B. Aggregated and monomeric alpha-synuclein bind to the S6′ proteasomal protein and inhibit proteasomal function. J. Biol. Chem. 278 14 (2003) 11753-11759
    • (2003) J. Biol. Chem. , vol.278 , Issue.14 , pp. 11753-11759
    • Snyder, H.1    Mensah, K.2    Theisler, C.3    Lee, J.4    Matouschek, A.5    Wolozin, B.6
  • 136
    • 50649112184 scopus 로고    scopus 로고
    • alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis
    • Zhang N.Y., Tang Z., and Liu C.W. alpha-Synuclein protofibrils inhibit 26 S proteasome-mediated protein degradation: understanding the cytotoxicity of protein protofibrils in neurodegenerative disease pathogenesis. J. Biol. Chem. 283 29 (2008) 20288-20298
    • (2008) J. Biol. Chem. , vol.283 , Issue.29 , pp. 20288-20298
    • Zhang, N.Y.1    Tang, Z.2    Liu, C.W.3
  • 137
    • 0033788434 scopus 로고    scopus 로고
    • Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex
    • Ghee M., Fournier A., and Mallet J. Rat alpha-synuclein interacts with Tat binding protein 1, a component of the 26S proteasomal complex. J. Neurochem. 75 5 (2000) 2221-2224
    • (2000) J. Neurochem. , vol.75 , Issue.5 , pp. 2221-2224
    • Ghee, M.1    Fournier, A.2    Mallet, J.3
  • 138
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R., Head E., Thompson J.L., McIntire T.M., Milton S.C., Cotman C.W., et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 5618 (2003) 486-489
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6
  • 139
    • 51449096696 scopus 로고    scopus 로고
    • Abeta inhibits the proteasome and enhances amyloid and tau accumulation
    • Tseng B.P., Green K.N., Chan J.L., Blurton-Jones M., and Laferla F.M. Abeta inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiol. Aging 29 11 (2008) 1607-1618
    • (2008) Neurobiol. Aging , vol.29 , Issue.11 , pp. 1607-1618
    • Tseng, B.P.1    Green, K.N.2    Chan, J.L.3    Blurton-Jones, M.4    Laferla, F.M.5
  • 140
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence N.F., Sampat R.M., and Kopito R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 292 5521 (2001) 1552-1555
    • (2001) Science , vol.292 , Issue.5521 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 141
    • 13244258435 scopus 로고    scopus 로고
    • Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation
    • Bennett E.J., Bence N.F., Jayakumar R., and Kopito R.R. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol. Cell 17 3 (2005) 351-365
    • (2005) Mol. Cell , vol.17 , Issue.3 , pp. 351-365
    • Bennett, E.J.1    Bence, N.F.2    Jayakumar, R.3    Kopito, R.R.4
  • 143
    • 0035336658 scopus 로고    scopus 로고
    • Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release
    • Jana N.R., Zemskov E.A., Wang G., and Nukina N. Altered proteasomal function due to the expression of polyglutamine-expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release. Hum. Mol. Genet. 10 10 (2001) 1049-1059
    • (2001) Hum. Mol. Genet. , vol.10 , Issue.10 , pp. 1049-1059
    • Jana, N.R.1    Zemskov, E.A.2    Wang, G.3    Nukina, N.4
  • 144
    • 0037108725 scopus 로고    scopus 로고
    • Aggregate formation inhibits proteasomal degradation of polyglutamine proteins
    • Verhoef L.G., Lindsten K., Masucci M.G., and Dantuma N.P. Aggregate formation inhibits proteasomal degradation of polyglutamine proteins. Hum. Mol. Genet. 11 22 (2002) 2689-2700
    • (2002) Hum. Mol. Genet. , vol.11 , Issue.22 , pp. 2689-2700
    • Verhoef, L.G.1    Lindsten, K.2    Masucci, M.G.3    Dantuma, N.P.4
  • 146
    • 0037173006 scopus 로고    scopus 로고
    • Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice
    • Lee M.K., Stirling W., Xu Y., Xu X., Qui D., Mandir A.S., et al. Human alpha-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with alpha-synuclein aggregation in transgenic mice. Proc. Natl. Acad. Sci. U. S. A. 99 13 (2002) 8968-8973
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.13 , pp. 8968-8973
    • Lee, M.K.1    Stirling, W.2    Xu, Y.3    Xu, X.4    Qui, D.5    Mandir, A.S.6
  • 147
    • 0034517732 scopus 로고    scopus 로고
    • Importance of familial Parkinson's disease and parkinsonism to the understanding of nigral degeneration in sporadic Parkinson's disease
    • Hattori N., Shimura H., Kubo S., Wang M., Shimizu N., Tanaka K., et al. Importance of familial Parkinson's disease and parkinsonism to the understanding of nigral degeneration in sporadic Parkinson's disease. J. Neural Transm., Suppl. 60 (2000) 101-116
    • (2000) J. Neural Transm., Suppl. , vol.60 , pp. 101-116
    • Hattori, N.1    Shimura, H.2    Kubo, S.3    Wang, M.4    Shimizu, N.5    Tanaka, K.6
  • 148
    • 0342368772 scopus 로고    scopus 로고
    • Association between early-onset Parkinson's disease and mutations in the parkin gene
    • Lucking C.B., Durr A., Bonifati V., Vaughan J., De Michele G., Gasser T., et al. Association between early-onset Parkinson's disease and mutations in the parkin gene. N. Engl. J. Med. 342 21 (2000) 1560-1567
    • (2000) N. Engl. J. Med. , vol.342 , Issue.21 , pp. 1560-1567
    • Lucking, C.B.1    Durr, A.2    Bonifati, V.3    Vaughan, J.4    De Michele, G.5    Gasser, T.6
  • 149
    • 1842455356 scopus 로고    scopus 로고
    • Parkin genetics: one model for Parkinson's disease
    • Mata I.F., Lockhart P.J., and Farrer M.J. Parkin genetics: one model for Parkinson's disease. Hum. Mol. Genet. 13 Spec No 1 (2004) R127-R133
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.Spec No 1
    • Mata, I.F.1    Lockhart, P.J.2    Farrer, M.J.3
  • 150
    • 0033814671 scopus 로고    scopus 로고
    • An autopsy case of autosomal-recessive juvenile parkinsonism with a homozygous exon 4 deletion in the parkin gene
    • Hayashi S., Wakabayashi K., Ishikawa A., Nagai H., Saito M., Maruyama M., et al. An autopsy case of autosomal-recessive juvenile parkinsonism with a homozygous exon 4 deletion in the parkin gene. Mov. Disord. 15 5 (2000) 884-888
    • (2000) Mov. Disord. , vol.15 , Issue.5 , pp. 884-888
    • Hayashi, S.1    Wakabayashi, K.2    Ishikawa, A.3    Nagai, H.4    Saito, M.5    Maruyama, M.6
  • 151
    • 0031721141 scopus 로고    scopus 로고
    • Pathologic and biochemical studies of juvenile parkinsonism linked to chromosome 6q
    • Mori H., Kondo T., Yokochi M., Matsumine H., Nakagawa-Hattori Y., Miyake T., et al. Pathologic and biochemical studies of juvenile parkinsonism linked to chromosome 6q. Neurology 51 3 (1998) 890-892
    • (1998) Neurology , vol.51 , Issue.3 , pp. 890-892
    • Mori, H.1    Kondo, T.2    Yokochi, M.3    Matsumine, H.4    Nakagawa-Hattori, Y.5    Miyake, T.6
  • 152
    • 0028198309 scopus 로고
    • Familial juvenile parkinsonism: clinical and pathologic study in a family
    • Takahashi H., Ohama E., Suzuki S., Horikawa Y., Ishikawa A., Morita T., et al. Familial juvenile parkinsonism: clinical and pathologic study in a family. Neurology 44 3 Pt 1 (1994) 437-441
    • (1994) Neurology , vol.44 , Issue.3 PART 1 , pp. 437-441
    • Takahashi, H.1    Ohama, E.2    Suzuki, S.3    Horikawa, Y.4    Ishikawa, A.5    Morita, T.6
  • 153
    • 0035957112 scopus 로고    scopus 로고
    • Clinical and pathologic abnormalities in a family with parkinsonism and parkin gene mutations
    • van de Warrenburg B.P., Lammens M., Lucking C.B., Denefle P., Wesseling P., Booij J., et al. Clinical and pathologic abnormalities in a family with parkinsonism and parkin gene mutations. Neurology 56 4 (2001) 555-557
    • (2001) Neurology , vol.56 , Issue.4 , pp. 555-557
    • van de Warrenburg, B.P.1    Lammens, M.2    Lucking, C.B.3    Denefle, P.4    Wesseling, P.5    Booij, J.6
  • 154
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y., Soda M., Inoue H., Hattori N., Mizuno Y., and Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105 7 (2001) 891-902
    • (2001) Cell , vol.105 , Issue.7 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 155
    • 0037422010 scopus 로고    scopus 로고
    • Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity
    • Staropoli J.F., McDermott C., Martinat C., Schulman B., Demireva E., and Abeliovich A. Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity. Neuron 37 5 (2003) 735-749
    • (2003) Neuron , vol.37 , Issue.5 , pp. 735-749
    • Staropoli, J.F.1    McDermott, C.2    Martinat, C.3    Schulman, B.4    Demireva, E.5    Abeliovich, A.6
  • 156
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease
    • Shimura H., Schlossmacher M.G., Hattori N., Frosch M.P., Trockenbacher A., Schneider R., et al. Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 293 5528 (2001) 263-269
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6
  • 158
    • 43749102944 scopus 로고    scopus 로고
    • alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease
    • Kawahara K., Hashimoto M., Bar-On P., Ho G.J., Crews L., Mizuno H., et al. alpha-Synuclein aggregates interfere with Parkin solubility and distribution: role in the pathogenesis of Parkinson disease. J. Biol. Chem. 283 11 (2008) 6979-6987
    • (2008) J. Biol. Chem. , vol.283 , Issue.11 , pp. 6979-6987
    • Kawahara, K.1    Hashimoto, M.2    Bar-On, P.3    Ho, G.J.4    Crews, L.5    Mizuno, H.6
  • 160
    • 4444370179 scopus 로고    scopus 로고
    • How does parkin ligate ubiquitin to Parkinson's disease?
    • Kahle P.J., and Haass C. How does parkin ligate ubiquitin to Parkinson's disease?. EMBO Rep. 5 7 (2004) 681-685
    • (2004) EMBO Rep. , vol.5 , Issue.7 , pp. 681-685
    • Kahle, P.J.1    Haass, C.2
  • 161
    • 18044364423 scopus 로고    scopus 로고
    • Pathological proteins in Parkinson's disease: focus on the proteasome
    • Snyder H., and Wolozin B. Pathological proteins in Parkinson's disease: focus on the proteasome. J. Mol. Neurosci. 24 3 (2004) 425-442
    • (2004) J. Mol. Neurosci. , vol.24 , Issue.3 , pp. 425-442
    • Snyder, H.1    Wolozin, B.2
  • 162
    • 0034700158 scopus 로고    scopus 로고
    • Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
    • Zhang Y., Gao J., Chung K.K., Huang H., Dawson V.L., and Dawson T.M. Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc. Natl. Acad. Sci. U. S. A. 97 24 (2000) 13354-13359
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , Issue.24 , pp. 13354-13359
    • Zhang, Y.1    Gao, J.2    Chung, K.K.3    Huang, H.4    Dawson, V.L.5    Dawson, T.M.6
  • 163
    • 27944506923 scopus 로고    scopus 로고
    • A Caenorhabditis elegans Parkin mutant with altered solubility couples alpha-synuclein aggregation to proteotoxic stress
    • Springer W., Hoppe T., Schmidt E., and Baumeister R. A Caenorhabditis elegans Parkin mutant with altered solubility couples alpha-synuclein aggregation to proteotoxic stress. Hum. Mol. Genet. 14 22 (2005) 3407-3423
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.22 , pp. 3407-3423
    • Springer, W.1    Hoppe, T.2    Schmidt, E.3    Baumeister, R.4
  • 164
    • 46649117176 scopus 로고    scopus 로고
    • Aberrant folding of pathogenic Parkin mutants: aggregation versus degradation
    • Schlehe J.S., Lutz A.K., Pilsl A., Lammermann K., Grgur K., Henn I.H., et al. Aberrant folding of pathogenic Parkin mutants: aggregation versus degradation. J. Biol. Chem. 283 20 (2008) 13771-13779
    • (2008) J. Biol. Chem. , vol.283 , Issue.20 , pp. 13771-13779
    • Schlehe, J.S.1    Lutz, A.K.2    Pilsl, A.3    Lammermann, K.4    Grgur, K.5    Henn, I.H.6
  • 165
    • 20244370595 scopus 로고    scopus 로고
    • Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations
    • Wang C., Tan J.M., Ho M.W., Zaiden N., Wong S.H., Chew C.L., et al. Alterations in the solubility and intracellular localization of parkin by several familial Parkinson's disease-linked point mutations. J. Neurochem. 93 2 (2005) 422-431
    • (2005) J. Neurochem. , vol.93 , Issue.2 , pp. 422-431
    • Wang, C.1    Tan, J.M.2    Ho, M.W.3    Zaiden, N.4    Wong, S.H.5    Chew, C.L.6
  • 166
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung K.K., Thomas B., Li X., Pletnikova O., Troncoso J.C., Marsh L., et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304 5675 (2004) 1328-1331
    • (2004) Science , vol.304 , Issue.5675 , pp. 1328-1331
    • Chung, K.K.1    Thomas, B.2    Li, X.3    Pletnikova, O.4    Troncoso, J.C.5    Marsh, L.6
  • 167
    • 10744224951 scopus 로고    scopus 로고
    • Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age
    • Pawlyk A.C., Giasson B.I., Sampathu D.M., Perez F.A., Lim K.L., Dawson V.L., et al. Novel monoclonal antibodies demonstrate biochemical variation of brain parkin with age. J. Biol. Chem. 278 48 (2003) 48120-48128
    • (2003) J. Biol. Chem. , vol.278 , Issue.48 , pp. 48120-48128
    • Pawlyk, A.C.1    Giasson, B.I.2    Sampathu, D.M.3    Perez, F.A.4    Lim, K.L.5    Dawson, V.L.6
  • 168
    • 0037338634 scopus 로고    scopus 로고
    • Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death
    • Darios F., Corti O., Lucking C.B., Hampe C., Muriel M.P., Abbas N., et al. Parkin prevents mitochondrial swelling and cytochrome c release in mitochondria-dependent cell death. Hum. Mol. Genet. 12 5 (2003) 517-526
    • (2003) Hum. Mol. Genet. , vol.12 , Issue.5 , pp. 517-526
    • Darios, F.1    Corti, O.2    Lucking, C.B.3    Hampe, C.4    Muriel, M.P.5    Abbas, N.6
  • 170
    • 0034680913 scopus 로고    scopus 로고
    • Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
    • Imai Y., Soda M., and Takahashi R. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J. Biol. Chem. 275 46 (2000) 35661-35664
    • (2000) J. Biol. Chem. , vol.275 , Issue.46 , pp. 35661-35664
    • Imai, Y.1    Soda, M.2    Takahashi, R.3
  • 171
    • 4444327827 scopus 로고    scopus 로고
    • Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis
    • Jiang H., Ren Y., Zhao J., and Feng J. Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis. Hum. Mol. Genet. 13 16 (2004) 1745-1754
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.16 , pp. 1745-1754
    • Jiang, H.1    Ren, Y.2    Zhao, J.3    Feng, J.4
  • 172
    • 24144497601 scopus 로고    scopus 로고
    • Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death
    • Ko H.S., von Coelln R., Sriram S.R., Kim S.W., Chung K.K., Pletnikova O., et al. Accumulation of the authentic parkin substrate aminoacyl-tRNA synthetase cofactor, p38/JTV-1, leads to catecholaminergic cell death. J. Neurosci. 25 35 (2005) 7968-7978
    • (2005) J. Neurosci. , vol.25 , Issue.35 , pp. 7968-7978
    • Ko, H.S.1    von Coelln, R.2    Sriram, S.R.3    Kim, S.W.4    Chung, K.K.5    Pletnikova, O.6
  • 173
    • 0036902707 scopus 로고    scopus 로고
    • Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress
    • Ledesma M.D., Galvan C., Hellias B., Dotti C., and Jensen P.H. Astrocytic but not neuronal increased expression and redistribution of parkin during unfolded protein stress. J. Neurochem. 83 6 (2002) 1431-1440
    • (2002) J. Neurochem. , vol.83 , Issue.6 , pp. 1431-1440
    • Ledesma, M.D.1    Galvan, C.2    Hellias, B.3    Dotti, C.4    Jensen, P.H.5
  • 174
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., Fishman P.S., Thakor N.V., and Oyler G.A. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J. Biol. Chem. 278 24 (2003) 22044-22055
    • (2003) J. Biol. Chem. , vol.278 , Issue.24 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 175
    • 0037468831 scopus 로고    scopus 로고
    • Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila
    • Yang Y., Nishimura I., Imai Y., Takahashi R., and Lu B. Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron 37 6 (2003) 911-924
    • (2003) Neuron , vol.37 , Issue.6 , pp. 911-924
    • Yang, Y.1    Nishimura, I.2    Imai, Y.3    Takahashi, R.4    Lu, B.5
  • 176
    • 20344369560 scopus 로고    scopus 로고
    • Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease
    • Whitworth A.J., Theodore D.A., Greene J.C., Benes H., Wes P.D., and Pallanck L.J. Increased glutathione S-transferase activity rescues dopaminergic neuron loss in a Drosophila model of Parkinson's disease. Proc. Natl. Acad. Sci. U. S. A. 102 22 (2005) 8024-8029
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.22 , pp. 8024-8029
    • Whitworth, A.J.1    Theodore, D.A.2    Greene, J.C.3    Benes, H.4    Wes, P.D.5    Pallanck, L.J.6
  • 177
    • 30044449754 scopus 로고    scopus 로고
    • DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T alpha-synuclein toxicity
    • Zhou W., and Freed C.R. DJ-1 up-regulates glutathione synthesis during oxidative stress and inhibits A53T alpha-synuclein toxicity. J. Biol. Chem. 280 52 (2005) 43150-43158
    • (2005) J. Biol. Chem. , vol.280 , Issue.52 , pp. 43150-43158
    • Zhou, W.1    Freed, C.R.2
  • 179
    • 50549103561 scopus 로고    scopus 로고
    • Death receptors and caspases but not mitochondria are activated in the GDNF- or BDNF-deprived dopaminergic neurons
    • Yu L.Y., Saarma M., and Arumae U. Death receptors and caspases but not mitochondria are activated in the GDNF- or BDNF-deprived dopaminergic neurons. J. Neurosci. 28 30 (2008) 7467-7475
    • (2008) J. Neurosci. , vol.28 , Issue.30 , pp. 7467-7475
    • Yu, L.Y.1    Saarma, M.2    Arumae, U.3
  • 181
    • 0034959811 scopus 로고    scopus 로고
    • Depletion of glial cell line-derived neurotrophic factor in substantia nigra neurons of Parkinson's disease brain
    • Chauhan N.B., Siegel G.J., and Lee J.M. Depletion of glial cell line-derived neurotrophic factor in substantia nigra neurons of Parkinson's disease brain. J. Chem. Neuroanat. 21 4 (2001) 277-288
    • (2001) J. Chem. Neuroanat. , vol.21 , Issue.4 , pp. 277-288
    • Chauhan, N.B.1    Siegel, G.J.2    Lee, J.M.3
  • 182
    • 0033813571 scopus 로고    scopus 로고
    • Neurotrophic factors in Alzheimer's and Parkinson's disease brain
    • Siegel G.J., and Chauhan N.B. Neurotrophic factors in Alzheimer's and Parkinson's disease brain. Brain Res. Brain Res. Rev. 33 2-3 (2000) 199-227
    • (2000) Brain Res. Brain Res. Rev. , vol.33 , Issue.2-3 , pp. 199-227
    • Siegel, G.J.1    Chauhan, N.B.2
  • 183
    • 37049015753 scopus 로고    scopus 로고
    • Induction of neurotrophic factors GDNF and BDNF associated with the mechanism of neurorescue action of rasagiline and ladostigil: new insights and implications for therapy
    • Weinreb O., Amit T., Bar-Am O., and Youdim M.B. Induction of neurotrophic factors GDNF and BDNF associated with the mechanism of neurorescue action of rasagiline and ladostigil: new insights and implications for therapy. Ann. N.Y. Acad. Sci. 1122 (2007) 155-168
    • (2007) Ann. N.Y. Acad. Sci. , vol.1122 , pp. 155-168
    • Weinreb, O.1    Amit, T.2    Bar-Am, O.3    Youdim, M.B.4
  • 184
    • 0032957883 scopus 로고    scopus 로고
    • Immunohistochemical and subcellular localization of Parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients
    • Shimura H., Hattori N., Kubo S., Yoshikawa M., Kitada T., Matsumine H., et al. Immunohistochemical and subcellular localization of Parkin protein: absence of protein in autosomal recessive juvenile parkinsonism patients. Ann. Neurol. 45 5 (1999) 668-672
    • (1999) Ann. Neurol. , vol.45 , Issue.5 , pp. 668-672
    • Shimura, H.1    Hattori, N.2    Kubo, S.3    Yoshikawa, M.4    Kitada, T.5    Matsumine, H.6
  • 186
    • 0035813135 scopus 로고    scopus 로고
    • DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor
    • Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M., and Ariga H. DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J. Biol. Chem. 276 40 (2001) 37556-37563
    • (2001) J. Biol. Chem. , vol.276 , Issue.40 , pp. 37556-37563
    • Takahashi, K.1    Taira, T.2    Niki, T.3    Seino, C.4    Iguchi-Ariga, S.M.5    Ariga, H.6
  • 187
    • 20944437573 scopus 로고    scopus 로고
    • The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
    • Xu J., Zhong N., Wang H., Elias J.E., Kim C.Y., Woldman I., et al. The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis. Hum. Mol. Genet. 14 9 (2005) 1231-1241
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.9 , pp. 1231-1241
    • Xu, J.1    Zhong, N.2    Wang, H.3    Elias, J.E.4    Kim, C.Y.5    Woldman, I.6
  • 188
    • 33746355607 scopus 로고    scopus 로고
    • DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor
    • Zhong N., Kim C.Y., Rizzu P., Geula C., Porter D.R., Pothos E.N., et al. DJ-1 transcriptionally up-regulates the human tyrosine hydroxylase by inhibiting the sumoylation of pyrimidine tract-binding protein-associated splicing factor. J. Biol. Chem. 281 30 (2006) 20940-20948
    • (2006) J. Biol. Chem. , vol.281 , Issue.30 , pp. 20940-20948
    • Zhong, N.1    Kim, C.Y.2    Rizzu, P.3    Geula, C.4    Porter, D.R.5    Pothos, E.N.6
  • 189
  • 190
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J., Krieger E., et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299 5604 (2003) 256-259
    • (2003) Science , vol.299 , Issue.5604 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    van Baren, M.J.3    Schaap, O.4    Breedveld, G.J.5    Krieger, E.6
  • 192
    • 0043204995 scopus 로고    scopus 로고
    • Early-onset Parkinson's disease caused by a compound heterozygous DJ-1 mutation
    • Hague S., Rogaeva E., Hernandez D., Gulick C., Singleton A., Hanson M., et al. Early-onset Parkinson's disease caused by a compound heterozygous DJ-1 mutation. Ann. Neurol. 54 2 (2003) 271-274
    • (2003) Ann. Neurol. , vol.54 , Issue.2 , pp. 271-274
    • Hague, S.1    Rogaeva, E.2    Hernandez, D.3    Gulick, C.4    Singleton, A.5    Hanson, M.6
  • 193
    • 13944267769 scopus 로고    scopus 로고
    • DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation
    • Shendelman S., Jonason A., Martinat C., Leete T., and Abeliovich A. DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol. 2 11 (2004) e362
    • (2004) PLoS Biol. , vol.2 , Issue.11
    • Shendelman, S.1    Jonason, A.2    Martinat, C.3    Leete, T.4    Abeliovich, A.5
  • 194
    • 13944279784 scopus 로고    scopus 로고
    • Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES-derived cell model of primary Parkinsonism
    • Martinat C., Shendelman S., Jonason A., Leete T., Beal M.F., Yang L., et al. Sensitivity to oxidative stress in DJ-1-deficient dopamine neurons: an ES-derived cell model of primary Parkinsonism. PLoS Biol. 2 11 (2004) e327
    • (2004) PLoS Biol. , vol.2 , Issue.11
    • Martinat, C.1    Shendelman, S.2    Jonason, A.3    Leete, T.4    Beal, M.F.5    Yang, L.6
  • 195
    • 0345357664 scopus 로고    scopus 로고
    • Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition
    • Yokota T., Sugawara K., Ito K., Takahashi R., Ariga H., and Mizusawa H. Down regulation of DJ-1 enhances cell death by oxidative stress, ER stress, and proteasome inhibition. Biochem. Biophys. Res. Commun. 312 4 (2003) 1342-1348
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , Issue.4 , pp. 1342-1348
    • Yokota, T.1    Sugawara, K.2    Ito, K.3    Takahashi, R.4    Ariga, H.5    Mizusawa, H.6
  • 196
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J., Dexter D.T., Lees A.J., Daniel S., Agid Y., Javoy-Agid F., et al. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann. Neurol. 36 3 (1994) 348-355
    • (1994) Ann. Neurol. , vol.36 , Issue.3 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6
  • 198
    • 38449097902 scopus 로고    scopus 로고
    • Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons result in nigrostriatal degeneration
    • Chinta S.J., Kumar M.J., Hsu M., Rajagopalan S., Kaur D., Rane A., et al. Inducible alterations of glutathione levels in adult dopaminergic midbrain neurons result in nigrostriatal degeneration. J. Neurosci. 27 51 (2007) 13997-14006
    • (2007) J. Neurosci. , vol.27 , Issue.51 , pp. 13997-14006
    • Chinta, S.J.1    Kumar, M.J.2    Hsu, M.3    Rajagopalan, S.4    Kaur, D.5    Rane, A.6
  • 199
    • 33646796739 scopus 로고    scopus 로고
    • In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease
    • Chinta S.J., Rajagopalan S., Butterfield D.A., and Andersen J.K. In vitro and in vivo neuroprotection by gamma-glutamylcysteine ethyl ester against MPTP: relevance to the role of glutathione in Parkinson's disease. Neurosci. Lett. 402 1-2 (2006) 137-141
    • (2006) Neurosci. Lett. , vol.402 , Issue.1-2 , pp. 137-141
    • Chinta, S.J.1    Rajagopalan, S.2    Butterfield, D.A.3    Andersen, J.K.4
  • 200
    • 14644416354 scopus 로고    scopus 로고
    • Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: implications for Parkinson's disease
    • Hsu M., Srinivas B., Kumar J., Subramanian R., and Andersen J. Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: implications for Parkinson's disease. J. Neurochem. 92 5 (2005) 1091-1103
    • (2005) J. Neurochem. , vol.92 , Issue.5 , pp. 1091-1103
    • Hsu, M.1    Srinivas, B.2    Kumar, J.3    Subramanian, R.4    Andersen, J.5
  • 201
    • 0242721624 scopus 로고    scopus 로고
    • Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway
    • Kwak M.K., Wakabayashi N., Greenlaw J.L., Yamamoto M., and Kensler T.W. Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell. Biol. 23 23 (2003) 8786-8794
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.23 , pp. 8786-8794
    • Kwak, M.K.1    Wakabayashi, N.2    Greenlaw, J.L.3    Yamamoto, M.4    Kensler, T.W.5
  • 202
    • 0031577292 scopus 로고    scopus 로고
    • An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements
    • Itoh K., Chiba T., Takahashi S., Ishii T., Igarashi K., Katoh Y., et al. An Nrf2/small Maf heterodimer mediates the induction of phase II detoxifying enzyme genes through antioxidant response elements. Biochem. Biophys. Res. Commun. 236 2 (1997) 313-322
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , Issue.2 , pp. 313-322
    • Itoh, K.1    Chiba, T.2    Takahashi, S.3    Ishii, T.4    Igarashi, K.5    Katoh, Y.6
  • 203
    • 0035260034 scopus 로고    scopus 로고
    • Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione
    • Kwak M.K., Itoh K., Yamamoto M., Sutter T.R., and Kensler T.W. Role of transcription factor Nrf2 in the induction of hepatic phase 2 and antioxidative enzymes in vivo by the cancer chemoprotective agent, 3H-1, 2-dimethiole-3-thione. Mol. Med. 7 2 (2001) 135-145
    • (2001) Mol. Med. , vol.7 , Issue.2 , pp. 135-145
    • Kwak, M.K.1    Itoh, K.2    Yamamoto, M.3    Sutter, T.R.4    Kensler, T.W.5
  • 204
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa R.K., Mai K.H., Srisuma S., Kensler T.W., Yamamoto M., and Biswal S. Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray. Cancer Res. 62 18 (2002) 5196-5203
    • (2002) Cancer Res. , vol.62 , Issue.18 , pp. 5196-5203
    • Thimmulappa, R.K.1    Mai, K.H.2    Srisuma, S.3    Kensler, T.W.4    Yamamoto, M.5    Biswal, S.6
  • 205
  • 206
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K., Wakabayashi N., Katoh Y., Ishii T., Igarashi K., Engel J.D., et al. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13 1 (1999) 76-86
    • (1999) Genes Dev. , vol.13 , Issue.1 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6
  • 207
    • 33750052885 scopus 로고    scopus 로고
    • DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2
    • Clements C.M., McNally R.S., Conti B.J., Mak T.W., and Ting J.P. DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc. Natl. Acad. Sci. U. S. A. 103 41 (2006) 15091-15096
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , Issue.41 , pp. 15091-15096
    • Clements, C.M.1    McNally, R.S.2    Conti, B.J.3    Mak, T.W.4    Ting, J.P.5
  • 208
    • 0037462651 scopus 로고    scopus 로고
    • Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium
    • Stewart D., Killeen E., Naquin R., Alam S., and Alam J. Degradation of transcription factor Nrf2 via the ubiquitin-proteasome pathway and stabilization by cadmium. J. Biol. Chem. 278 4 (2003) 2396-2402
    • (2003) J. Biol. Chem. , vol.278 , Issue.4 , pp. 2396-2402
    • Stewart, D.1    Killeen, E.2    Naquin, R.3    Alam, S.4    Alam, J.5
  • 209
    • 35748954034 scopus 로고    scopus 로고
    • Paraquat induces dopaminergic dysfunction and proteasome impairment in DJ-1-deficient mice
    • Yang W., Chen L., Ding Y., Zhuang X., and Kang U.J. Paraquat induces dopaminergic dysfunction and proteasome impairment in DJ-1-deficient mice. Hum. Mol. Genet. 16 23 (2007) 2900-2910
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.23 , pp. 2900-2910
    • Yang, W.1    Chen, L.2    Ding, Y.3    Zhuang, X.4    Kang, U.J.5
  • 210
    • 42549123597 scopus 로고    scopus 로고
    • LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease
    • Alegre-Abarrategui J., Ansorge O., Esiri M., and Wade-Martins R. LRRK2 is a component of granular alpha-synuclein pathology in the brainstem of Parkinson's disease. Neuropathol. Appl. Neurobiol. 34 3 (2008) 272-283
    • (2008) Neuropathol. Appl. Neurobiol. , vol.34 , Issue.3 , pp. 272-283
    • Alegre-Abarrategui, J.1    Ansorge, O.2    Esiri, M.3    Wade-Martins, R.4
  • 211
    • 40449088676 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 colocalizes with alpha-synuclein in Parkinson's disease, but not tau-containing deposits in tauopathies
    • Perry G., Zhu X., Babar A.K., Siedlak S.L., Yang Q., Ito G., et al. Leucine-rich repeat kinase 2 colocalizes with alpha-synuclein in Parkinson's disease, but not tau-containing deposits in tauopathies. Neurodegener. Dis. 5 3-4 (2008) 222-224
    • (2008) Neurodegener. Dis. , vol.5 , Issue.3-4 , pp. 222-224
    • Perry, G.1    Zhu, X.2    Babar, A.K.3    Siedlak, S.L.4    Yang, Q.5    Ito, G.6
  • 212
    • 0036196860 scopus 로고    scopus 로고
    • A new locus for Parkinson's disease (PARK8) maps to chromosome 12p11.2-q13.1
    • Funayama M., Hasegawa K., Kowa H., Saito M., Tsuji S., and Obata F. A new locus for Parkinson's disease (PARK8) maps to chromosome 12p11.2-q13.1. Ann. Neurol. 51 3 (2002) 296-301
    • (2002) Ann. Neurol. , vol.51 , Issue.3 , pp. 296-301
    • Funayama, M.1    Hasegawa, K.2    Kowa, H.3    Saito, M.4    Tsuji, S.5    Obata, F.6
  • 216
    • 1842563060 scopus 로고    scopus 로고
    • Substantia nigra Marinesco bodies are associated with decreased striatal expression of dopaminergic markers
    • Beach T.G., Walker D.G., Sue L.I., Newell A., Adler C.C., and Joyce J.N. Substantia nigra Marinesco bodies are associated with decreased striatal expression of dopaminergic markers. J. Neuropathol. Exp. Neurol. 63 4 (2004) 329-337
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , Issue.4 , pp. 329-337
    • Beach, T.G.1    Walker, D.G.2    Sue, L.I.3    Newell, A.4    Adler, C.C.5    Joyce, J.N.6
  • 217
    • 29444437871 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration
    • Smith W.W., Pei Z., Jiang H., Moore D.J., Liang Y., West A.B., et al. Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc. Natl. Acad. Sci. U. S. A. 102 51 (2005) 18676-18681
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.51 , pp. 18676-18681
    • Smith, W.W.1    Pei, Z.2    Jiang, H.3    Moore, D.J.4    Liang, Y.5    West, A.B.6
  • 218
    • 31144443248 scopus 로고    scopus 로고
    • The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity
    • Gloeckner C.J., Kinkl N., Schumacher A., Braun R.J., O'Neill E., Meitinger T., et al. The Parkinson disease causing LRRK2 mutation I2020T is associated with increased kinase activity. Hum. Mol. Genet. 15 2 (2006) 223-232
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.2 , pp. 223-232
    • Gloeckner, C.J.1    Kinkl, N.2    Schumacher, A.3    Braun, R.J.4    O'Neill, E.5    Meitinger, T.6
  • 219
    • 28044460070 scopus 로고    scopus 로고
    • Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
    • West A.B., Moore D.J., Biskup S., Bugayenko A., Smith W.W., Ross C.A., et al. Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity. Proc. Natl. Acad. Sci. U. S. A. 102 46 (2005) 16842-16847
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.46 , pp. 16842-16847
    • West, A.B.1    Moore, D.J.2    Biskup, S.3    Bugayenko, A.4    Smith, W.W.5    Ross, C.A.6
  • 220
    • 41549144503 scopus 로고    scopus 로고
    • The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2
    • Wang L., Xie C., Greggio E., Parisiadou L., Shim H., Sun L., et al. The chaperone activity of heat shock protein 90 is critical for maintaining the stability of leucine-rich repeat kinase 2. J. Neurosci. 28 13 (2008) 3384-3391
    • (2008) J. Neurosci. , vol.28 , Issue.13 , pp. 3384-3391
    • Wang, L.1    Xie, C.2    Greggio, E.3    Parisiadou, L.4    Shim, H.5    Sun, L.6
  • 222
    • 33745068109 scopus 로고    scopus 로고
    • Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress
    • Muqit M.M., Abou-Sleiman P.M., Saurin A.T., Harvey K., Gandhi S., Deas E., et al. Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress. J. Neurochem. 98 1 (2006) 156-169
    • (2006) J. Neurochem. , vol.98 , Issue.1 , pp. 156-169
    • Muqit, M.M.1    Abou-Sleiman, P.M.2    Saurin, A.T.3    Harvey, K.4    Gandhi, S.5    Deas, E.6
  • 223
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L., Caputo V., Bellacchio E., Atorino L., Dallapiccola B., Valente E.M., et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum. Mol. Genet. 14 22 (2005) 3477-3492
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.22 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3    Atorino, L.4    Dallapiccola, B.5    Valente, E.M.6
  • 224
    • 2442668926 scopus 로고    scopus 로고
    • Hereditary early-onset Parkinson's disease caused by mutations in PINK1
    • Valente E.M., Abou-Sleiman P.M., Caputo V., Muqit M.M., Harvey K., Gispert S., et al. Hereditary early-onset Parkinson's disease caused by mutations in PINK1. Science 304 5674 (2004) 1158-1160
    • (2004) Science , vol.304 , Issue.5674 , pp. 1158-1160
    • Valente, E.M.1    Abou-Sleiman, P.M.2    Caputo, V.3    Muqit, M.M.4    Harvey, K.5    Gispert, S.6
  • 225
    • 33847622175 scopus 로고    scopus 로고
    • Biological effects of the PINK1 c.1366C>T mutation: implications in Parkinson disease pathogenesis
    • Grunewald A., Breedveld G.J., Lohmann-Hedrich K., Rohe C.F., Konig I.R., Hagenah J., et al. Biological effects of the PINK1 c.1366C>T mutation: implications in Parkinson disease pathogenesis. Neurogenetics 8 2 (2007) 103-109
    • (2007) Neurogenetics , vol.8 , Issue.2 , pp. 103-109
    • Grunewald, A.1    Breedveld, G.J.2    Lohmann-Hedrich, K.3    Rohe, C.F.4    Konig, I.R.5    Hagenah, J.6
  • 226
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A., Van Der Brug M., Ahmad R., Kesavapany S., Miller D.W., Petsko G.A., et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl. Acad. Sci. U. S. A. 102 16 (2005) 5703-5708
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , Issue.16 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6
  • 227
    • 33750220194 scopus 로고    scopus 로고
    • C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1
    • Sim C.H., Lio D.S., Mok S.S., Masters C.L., Hill A.F., Culvenor J.G., et al. C-terminal truncation and Parkinson's disease-associated mutations down-regulate the protein serine/threonine kinase activity of PTEN-induced kinase-1. Hum. Mol. Genet. 15 21 (2006) 3251-3262
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.21 , pp. 3251-3262
    • Sim, C.H.1    Lio, D.S.2    Mok, S.S.3    Masters, C.L.4    Hill, A.F.5    Culvenor, J.G.6
  • 228
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark I.E., Dodson M.W., Jiang C., Cao J.H., Huh J.R., Seol J.H., et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 7097 (2006) 1162-1166
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6
  • 229
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J., Lee S.B., Lee S., Kim Y., Song S., Kim S., et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 7097 (2006) 1157-1161
    • (2006) Nature , vol.441 , Issue.7097 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6
  • 231
    • 2542560342 scopus 로고    scopus 로고
    • Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress
    • Pesah Y., Pham T., Burgess H., Middlebrooks B., Verstreken P., Zhou Y., et al. Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress. Development 131 9 (2004) 2183-2194
    • (2004) Development , vol.131 , Issue.9 , pp. 2183-2194
    • Pesah, Y.1    Pham, T.2    Burgess, H.3    Middlebrooks, B.4    Verstreken, P.5    Zhou, Y.6
  • 232
    • 49349087497 scopus 로고    scopus 로고
    • PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons
    • Wood-Kaczmar A., Gandhi S., Yao Z., Abramov A.S., Miljan E.A., Keen G., et al. PINK1 is necessary for long term survival and mitochondrial function in human dopaminergic neurons. PLoS ONE 3 6 (2008) e2455
    • (2008) PLoS ONE , vol.3 , Issue.6
    • Wood-Kaczmar, A.1    Gandhi, S.2    Yao, Z.3    Abramov, A.S.4    Miljan, E.A.5    Keen, G.6
  • 233
    • 26644440926 scopus 로고    scopus 로고
    • Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations
    • Petit A., Kawarai T., Paitel E., Sanjo N., Maj M., Scheid M., et al. Wild-type PINK1 prevents basal and induced neuronal apoptosis, a protective effect abrogated by Parkinson disease-related mutations. J. Biol. Chem. 280 40 (2005) 34025-34032
    • (2005) J. Biol. Chem. , vol.280 , Issue.40 , pp. 34025-34032
    • Petit, A.1    Kawarai, T.2    Paitel, E.3    Sanjo, N.4    Maj, M.5    Scheid, M.6
  • 234
    • 35349030746 scopus 로고    scopus 로고
    • PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c
    • Wang H.L., Chou A.H., Yeh T.H., Li A.H., Chen Y.L., Kuo Y.L., et al. PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c. Neurobiol. Dis. 28 2 (2007) 216-226
    • (2007) Neurobiol. Dis. , vol.28 , Issue.2 , pp. 216-226
    • Wang, H.L.1    Chou, A.H.2    Yeh, T.H.3    Li, A.H.4    Chen, Y.L.5    Kuo, Y.L.6
  • 236
    • 4444274910 scopus 로고    scopus 로고
    • PINK1 mutations are associated with sporadic early-onset parkinsonism
    • Valente E.M., Salvi S., Ialongo T., Marongiu R., Elia A.E., Caputo V., et al. PINK1 mutations are associated with sporadic early-onset parkinsonism. Ann. Neurol. 56 3 (2004) 336-341
    • (2004) Ann. Neurol. , vol.56 , Issue.3 , pp. 336-341
    • Valente, E.M.1    Salvi, S.2    Ialongo, T.3    Marongiu, R.4    Elia, A.E.5    Caputo, V.6


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